5GGG

Crystal structure of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase form I

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008375	molecular_function	acetylglucosaminyltransferase activity
A	0009101	biological_process	glycoprotein biosynthetic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	161
Details	Domain: {"description":"GG-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU01375","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	13
Details	Region: {"description":"Interaction with O-glycosylated substrate glycoprotein","evidences":[{"source":"PubMed","id":"27493216","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27493216","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27493216","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"5GGI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27493216","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5GGI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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